In vitro protein folding by E. coli ribosome: unfolded protein splitting 70S to interact with 50S subunit

Basu, Arunima ; Samanta, Dibyendu ; Das, Debasis ; Chowdhury, Saheli ; Bhattacharya, Arpita ; Ghosh, Jaydip ; Das, Anindita ; DasGupta, Chanchal (2008) In vitro protein folding by E. coli ribosome: unfolded protein splitting 70S to interact with 50S subunit Biochemical and Biophysical Research Communications, 366 (2). pp. 598-603. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...

Related URL: http://dx.doi.org/10.1016/j.bbrc.2007.11.143

Abstract

Folding of unfolded protein on Escherichia coli 70S ribosome is accompanied by rapid dissociation of the ribosome into 50S and 30S subunits. The dissociation rate of 70S ribosome with unfolded protein is much faster than that caused by combined effect of translation and polypeptide release factors known to be involved in the dissociation of ribosome into subunits. The protein then reaches a "folding competent" state on 50S and is released to take up native conformation by itself. Release before attaining the folding competent state or prevention of release by cross-linking it with ribosome, would not allow the protein to get back to its native conformation.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:50s Subunit; Ribosomal Subunit Dissociation; Protein Folding
ID Code:8874
Deposited On:28 Oct 2010 10:41
Last Modified:28 May 2011 09:11

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